The permeability transition pore as a Ca2+ release channel: New answers to an old question (Articolo in rivista)

Type
Label
  • The permeability transition pore as a Ca2+ release channel: New answers to an old question (Articolo in rivista) (literal)
Anno
  • 2012-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1016/j.ceca.2012.03.004 (literal)
Alternative label
  • Bernardi, Paolo; von Stockum, Sophia (2012)
    The permeability transition pore as a Ca2+ release channel: New answers to an old question
    in Cell calcium (Edinburgh)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Bernardi, Paolo; von Stockum, Sophia (literal)
Pagina inizio
  • 22 (literal)
Pagina fine
  • 27 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#url
  • http://www.ncbi.nlm.nih.gov/pubmed/22513364 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 52 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#pagineTotali
  • 6 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
  • 1 (literal)
Note
  • ISI Web of Science (WOS) (literal)
  • Scopu (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Department of Biomedical Sciences and CNR Institute of Neuroscience, University of Padova, Padova, Italy (literal)
Titolo
  • The permeability transition pore as a Ca2+ release channel: New answers to an old question (literal)
Abstract
  • Mitochondria possess a sophisticated array of Ca2+ transport systems reflecting their key role in physiological Ca2+ homeostasis. With the exception of most yeast strains, energized organelles are endowed with a very fast and efficient mechanism for Ca2+ uptake, the ruthenium red (RR)-sensitive mitochondrial Ca2+ uniporter (MCU); and one main mechanism for Ca2+ release, the RR-insensitive 3Na(+)-Ca2+ antiporter. An additional mechanism for Ca2+ release is provided by a Na+ and RR-insensitive release mechanism, the putative 3H(+)-Ca2+ antiporter. A potential kinetic imbalance is present, however, because the V-max of the MCU is of the order of 1400 nmol Ca2+ mg(-1) protein min(-1) while the combined V-max of the efflux pathways is about 20 nmol Ca2+ mg(-1) protein min(-1). This arrangement exposes mitochondria to the hazards of Ca2+ overload when the rate of Ca2+ uptake exceeds that of the combined efflux pathways, e.g. for sharp increases of cytosolic [Ca2+]. In this short review we discuss the hypothesis that transient opening of the Ca2+-dependent permeability transition pore may provide mitocondria with a fast Ca2+ release channel preventing Ca2+ overload. We also address the relevance of a mitochondrial Ca2+ release channel recently discovered in Drosophila melanogaster, which possesses intermediate features between the permeability transition pore of yeast and mammals. (C) 2012 Elsevier Ltd. All rights reserved. (literal)
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